Selectivity of lipases and esterases towards phenol esters

被引:15
作者
Bornscheuer, UT
Ordoñez, GR
Hidalgo, A
Gollin, A
Lyon, J
Hitchman, TS
Weiner, DP
机构
[1] Ernst Moritz Arndt Univ Greifswald, Dept Tech Chem & Biotechnol, Inst Chem & Biochem, D-17487 Greifswald, Germany
[2] Diversa Corp, San Diego, CA 92121 USA
关键词
lipase; Gibbs' reagent; Hammett equation; esterase; phenol esters;
D O I
10.1016/j.molcatb.2005.07.004
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The selectivity of 28 lipases and esterases in the hydrolysis of butanoates of o-, m- or p-substituted phenols was investigated in a microtiter-plate format. The phenols released during enzyme-catalyzed hydrolysis were converted in situ with Gibbs' reagent to form a blue indophenol complex, which was quantified spectrophotometrically at 600 nm. Substantial differences in rates were found, which exhibits that the type and position of the substituent at the alkyl group has a strong influence on the selectivity of the enzymes. For various enzymes, the p-nitro derivative was the best substrate, whereas for other enzymes the m-Cl-derivative was preferentially hydrolyzed. Analysis of the data using the Hammett equation showed that sometimes the observed changes followed a predictable trend, but in several cases the result is very unexpected. (c) 2005 Elsevier B.V. All rights reserved.
引用
收藏
页码:8 / 13
页数:6
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